NDLI: Phosphatidylethanolamine-binding protein is not involved in µ-opioid receptor-mediated regulation of extracellular signal-regulated kinase.

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Phosphatidylethanolamine-binding protein is not involved in µ-opioid receptor-mediated regulation of extracellular signal-regulated kinase.

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Phosphatidylethanolamine-binding protein is not involved in µ-opioid receptor-mediated regulation of extracellular signal-regulated kinase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Su, Rui-Bin Wu, Ning Li, Jin Bian, Jia-Ming
Description	Author Affiliation: Bian JM ( State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Key Laboratory of Neuropsychopharmacology, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, P.R. China.); Wu N ( State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Key Laboratory of Neuropsychopharmacology, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, P.R. China.); Su RB ( State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Key Laboratory of Neuropsychopharmacology, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, P.R. China.); Li J ( State Key Laboratory of Toxicology and Medical Countermeasures, Beijing Key Laboratory of Neuropsychopharmacology, Beijing Institute of Pharmacology and Toxicology, Beijing 100850, P.R. China.)
Abstract	Stimulation of the µopioid receptor activates extracellular signalregulated kinase (ERK), however, the mechanism by which this occurs remains to be elucidated. Phosphatidylethanolaminebinding protein (PEBP) has been reported to act as a negative regulator of the ERK cascade (RafMEKERK) by binding to Raf1 kinase. In the present study, the role of PEBP in µopioid receptormediated ERK activation was investigated in Chinese hamster ovary/µ cells and SHSY5Y cells, as well as in human embryonic kidney 293 cells expressing other types of G proteincoupled receptors. The acute activation of µopioid receptors by morphine or (DAla2, MePhe4, Gly5ol) enkephalin induced a rapid activation of ERK. Prolonged morphine treatment did not affect the phosphorylation level of ERK compared with control cells, but the phosphorylation level of ERK decreased markedly when cells were precipitated with naloxone following chronic morphine treatment. For the phosphorylation of PEBP, no change was identified under the designated drug treatment and exposure duration. A total of two other types of G proteincoupled receptors, including Gscoupled dopamine D1 receptors and Gqcoupled adrenergic 1A receptors were also investigated and only the activation of adrenergic 1A receptors induced an upregulated phosphorylation of PEBP, which was protein kinase C activity dependent. Thus, PEBP did not have a significant role in µopioid receptormediated regulation of ERK.
ISSN	17912997
e-ISSN	17913004
DOI	10.3892/mmr.2015.3161
Journal	Molecular Medicine Reports
Issue Number	5
Volume Number	11
Language	English
Publisher	Spandidos Publications
Publisher Date	2015-05-01
Publisher Place	Greece
Access Restriction	Open
Subject Keyword	Extracellular Signal-regulated Map Kinases Metabolism Phosphatidylethanolamine Binding Protein Receptors, Opioid, Mu Analgesics, Opioid Pharmacology Animals Cho Cells Cell Line, Tumor Cricetinae Cricetulus Gene Expression Indoles Maleimides Morphine Genetics Phosphorylation Receptors, Adrenergic, Alpha-1 Receptors, Dopamine D1 Research Support, Non-u.s. Gov't Discipline Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Genetics Biochemistry Molecular Biology Cancer Research Molecular Medicine Oncology

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